L Scapozza
Biographic Data
| ID | 10773249 |
|---|---|
| NAME | L Scapozza |
| GIVEN NAMES | L |
| FAMILY NAME | Scapozza |
| SIGNATURE | SCAPOZZA L |
| AFFILIATIONS | Texas A&M University |
| VERIFIED | No |
| TOTAL WORKS | 1 |
| TOTAL CITATIONS | 0 |
| WORKS AS AUTHOR | 1 |
| WORKS AS EDITOR | 0 |
| FIRST PUBLICATION YEAR | 1996 |
| LATEST PUBLICATION YEAR | 1996 |
| H-INDEX | 0 |
Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Matrix metalloproteinase enzymes have been implicated in degenerative processes like tumor cell invasion, metastasis, and arthritis. Specific metalloproteinase inhibitors have been used to block tumor cell proliferation. We have examined the interaction of batimastat (BB-94) with a metalloproteinase [atrolysin C (Ht-d), EC 3.4.24.42] active site at 2.0-angstroms resolution (R = 16.8%). The title structure exhibits an unexpected binding geometry, …
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Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Matrix metalloproteinase enzymes have been implicated in degenerative processes like tumor cell invasion, metastasis, and arthritis. Specific metalloproteinase inhibitors have been used to block tumor cell proliferation. We have examined the interaction of batimastat (BB-94) with a metalloproteinase [atrolysin C (Ht-d), EC 3.4.24.42] active site at 2.0-angstroms resolution (R = 16.8%). The title structure exhibits an unexpected binding geometry, …
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